Heme oxygenase 1 (HO-1) modulates aerobic glycolysis through regulation of lactate dehydrogenase (LDH) in prostate cancer cells

CASCARDO, FLORENCIA; PAEZ ALEJANDRA; ANSELMINO NICOLAS; LABANCA ESTEFANIA; NAVONE NORA; GUERON GERALDINE; COTIGNOLA JAVIER; ELBA VAZQUEZ

Mar del Plata

Congreso; Reunión Anual de la Sociedad Argentina de Investigación Clínica 2019; 2019

Neoplastic proliferation requires tumour cells to reprogram their metabolic pathwaysin order to support the higher proliferation rate (known as the ?Warburg effect?). As a result,even under normal oxygen concentrations, transformed cells predominantly generate ATPthrough glycolysis followed by lactic acid fermentation, converting most incoming glucose tolactate rather than metabolizing it in the mitochondria through oxidative phosphorylation.We previously demonstrated that heme oxygenase 1 (HO-1), a cellular homeostaticregulator, has an antitumoral activity in prostate cancer (PCa) cells. In addition, aftertreatment with hemin, an inducer of HO-1 expression and activity, PC3 cells showedsignificantly lower glucose uptake, ATP production and oxygen consumption rate.In this context, we aimed to study whether HO-1 is involved in the regulation ofaerobic glycolysis through modulation of lactate dehydrogenase (LDH) in PC3, C4-2B and MDAPCa 2b cell lines under HO-1 induction with hemin (80 µM, 24h). We found a significantreduction in LDHA expression by RTqPCR (P